2gkw
From Proteopedia
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'''Key contacts promote recongnito of BAFF-R by TRAF3''' | '''Key contacts promote recongnito of BAFF-R by TRAF3''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ely, K R.]] | [[Category: Ely, K R.]] | ||
| - | [[Category: | + | [[Category: Baff receptor]] |
| - | [[Category: | + | [[Category: Cd40]] |
| - | [[Category: | + | [[Category: Nf-kb signaling]] |
| - | [[Category: | + | [[Category: Traf3]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:13:14 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:13, 4 May 2008
Key contacts promote recongnito of BAFF-R by TRAF3
Overview
B cell-activating factor belonging to the TNF family receptor (BAFF-R), a member of the TNFR superfamily, plays a role in autoimmunity after ligation with BAFF ligand (also called TALL-1, BLyS, THANK, or zTNF4). BAFF/BAFF-R interactions are critical for B cell regulation, and signaling from this ligand-receptor complex results in NF-kappaB activation. Most TNFRs transmit signals intracellularly by recruitment of adaptor proteins called TNFR-associated factors (TRAFs). However, BAFF-R binds only one TRAF adaptor, TRAF3, and this interaction negatively regulates activation of NF-kappaB. In this study, we report the crystal structure of a 24-residue fragment of the cytoplasmic portion of BAFF-R bound in complex with TRAF3. The recognition motif (162)PVPAT(166) in BAFF-R is accommodated in the same binding crevice on TRAF3 that binds two related TNFRs, CD40 and LTbetaR, but is presented in a completely different structural framework. This region of BAFF-R assumes an open conformation with two extended strands opposed at right angles that each make contacts with TRAF3. The recognition motif is located in the N-terminal arm and intermolecular contacts mediate TRAF recognition. In the C-terminal arm, key stabilizing contacts are made, including critical hydrogen bonds with Gln(379) in TRAF3 that define the molecular basis for selective binding of BAFF-R solely to this member of the TRAF family. A dynamic conformational adjustment of Tyr(377) in TRAF3 occurs forming a new intermolecular contact with BAFF-R that stabilizes the complex. The structure of the complex provides a molecular explanation for binding affinities and selective protein interactions in TNFR-TRAF interactions.
About this Structure
2GKW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Key molecular contacts promote recognition of the BAFF receptor by TNF receptor-associated factor 3: implications for intracellular signaling regulation., Ni CZ, Oganesyan G, Welsh K, Zhu X, Reed JC, Satterthwait AC, Cheng G, Ely KR, J Immunol. 2004 Dec 15;173(12):7394-400. PMID:15585864 Page seeded by OCA on Sun May 4 05:13:14 2008
